NIS1_YEAST
ID NIS1_YEAST Reviewed; 407 AA.
AC P53939; D6W1A1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein NIS1;
DE AltName: Full=Jumonji domain-interacting protein 1;
DE AltName: Full=Neck protein interacting with septins protein 1;
GN Name=NIS1; Synonyms=JIP1; OrderedLocusNames=YNL078W; ORFNames=N2337;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8701611;
RX DOI=10.1002/(sici)1097-0061(19960330)12:4<391::aid-yea921>3.0.co;2-n;
RA Poehlmann R., Philippsen P.;
RT "Sequencing a cosmid clone of Saccharomyces cerevisiae chromosome XIV
RT reveals 12 new open reading frames (ORFs) and an ancient duplication of six
RT ORFs.";
RL Yeast 12:391-402(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH SHS1 AND NAP1.
RX PubMed=11817649; DOI=10.1266/ggs.76.335;
RA Iwase M., Toh-e A.;
RT "Nis1 encoded by YNL078W: a new neck protein of Saccharomyces cerevisiae.";
RL Genes Genet. Syst. 76:335-343(2001).
RN [5]
RP INDUCTION.
RX PubMed=11309124; DOI=10.1046/j.1365-2958.2001.02388.x;
RA Doolin M.-T., Johnson A.L., Johnston L.H., Butler G.;
RT "Overlapping and distinct roles of the duplicated yeast transcription
RT factors Ace2p and Swi5p.";
RL Mol. Microbiol. 40:422-432(2001).
RN [6]
RP INTERACTION WITH PRM8.
RX PubMed=12101299; DOI=10.1099/00221287-148-7-2111;
RA Poirey R., Despons L., Leh V., Lafuente M.-J., Potier S., Souciet J.-L.,
RA Jauniaux J.-C.;
RT "Functional analysis of the Saccharomyces cerevisiae DUP240 multigene
RT family reveals membrane-associated proteins that are not essential for cell
RT viability.";
RL Microbiology 148:2111-2123(2002).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP INTERACTION WITH REI1, AND FUNCTION.
RX PubMed=15107529; DOI=10.1247/csf.29.1;
RA Iwase M., Toh-e A.;
RT "Ybr267w is a new cytoplasmic protein belonging to the mitotic signaling
RT network of Saccharomyces cerevisiae.";
RL Cell Struct. Funct. 29:1-15(2004).
RN [10]
RP INTERACTION WITH CBF2.
RX PubMed=16923829; DOI=10.1083/jcb.200605019;
RA Montpetit B., Hazbun T.R., Fields S., Hieter P.;
RT "Sumoylation of the budding yeast kinetochore protein Ndc10 is required for
RT Ndc10 spindle localization and regulation of anaphase spindle elongation.";
RL J. Cell Biol. 174:653-663(2006).
RN [11]
RP DOMAIN, AND INTERACTION WITH SUMOYLATED PROTEINS.
RX PubMed=17728242; DOI=10.1074/jbc.m706505200;
RA Uzunova K., Goettsche K., Miteva M., Weisshaar S.R., Glanemann C.,
RA Schnellhardt M., Niessen M., Scheel H., Hofmann K., Johnson E.S.,
RA Praefcke G.J.K., Dohmen R.J.;
RT "Ubiquitin-dependent proteolytic control of SUMO conjugates.";
RL J. Biol. Chem. 282:34167-34175(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [13]
RP INTERACTION WITH GIS1.
RX PubMed=17043893; DOI=10.1007/s00438-006-0171-3;
RA Tronnersjoe S., Hanefalk C., Balciunas D., Hu G.-Z., Nordberg N., Muren E.,
RA Ronne H.;
RT "The jmjN and jmjC domains of the yeast zinc finger protein Gis1 interact
RT with 19 proteins involved in transcription, sumoylation and DNA repair.";
RL Mol. Genet. Genomics 277:57-70(2007).
RN [14]
RP INTERACTION WITH NAP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18086883; DOI=10.1128/mcb.01035-07;
RA Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F.,
RA Pemberton L.F.;
RT "Phosphorylation by casein kinase 2 regulates Nap1 localization and
RT function.";
RL Mol. Cell. Biol. 28:1313-1325(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260; SER-264 AND SER-302, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: May be involved in a mitotic signaling network. Binds
CC sumoylated proteins and may stabilize SUMO chains.
CC {ECO:0000269|PubMed:15107529}.
CC -!- SUBUNIT: Interacts with CBF2, GIS1, NAP1, PRM8, REI1, SHS1 and SMT3.
CC {ECO:0000269|PubMed:11817649, ECO:0000269|PubMed:12101299,
CC ECO:0000269|PubMed:15107529, ECO:0000269|PubMed:16923829,
CC ECO:0000269|PubMed:17043893, ECO:0000269|PubMed:17728242,
CC ECO:0000269|PubMed:18086883}.
CC -!- INTERACTION:
CC P53939; Q99299: AIM44; NbExp=5; IntAct=EBI-28760, EBI-29423;
CC P53939; P25293: NAP1; NbExp=5; IntAct=EBI-28760, EBI-11850;
CC P53939; Q08229: NBA1; NbExp=3; IntAct=EBI-28760, EBI-36841;
CC -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:11817649}.
CC Cytoplasm, cell cortex {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Expression is regulated by the ACE2 and SWI5 transcription
CC factors. {ECO:0000269|PubMed:11309124}.
CC -!- MISCELLANEOUS: Present with 504 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X86470; CAA60180.1; -; Genomic_DNA.
DR EMBL; Z71354; CAA95952.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10467.1; -; Genomic_DNA.
DR PIR; S53900; S53900.
DR RefSeq; NP_014321.3; NM_001182916.3.
DR AlphaFoldDB; P53939; -.
DR BioGRID; 35745; 133.
DR DIP; DIP-1980N; -.
DR IntAct; P53939; 17.
DR MINT; P53939; -.
DR STRING; 4932.YNL078W; -.
DR iPTMnet; P53939; -.
DR MaxQB; P53939; -.
DR PaxDb; P53939; -.
DR PRIDE; P53939; -.
DR EnsemblFungi; YNL078W_mRNA; YNL078W; YNL078W.
DR GeneID; 855646; -.
DR KEGG; sce:YNL078W; -.
DR SGD; S000005022; NIS1.
DR VEuPathDB; FungiDB:YNL078W; -.
DR eggNOG; ENOG502SAJ9; Eukaryota.
DR HOGENOM; CLU_057191_0_0_1; -.
DR InParanoid; P53939; -.
DR OMA; IACKKGA; -.
DR BioCyc; YEAST:G3O-33107-MON; -.
DR PRO; PR:P53939; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53939; protein.
DR GO; GO:0032153; C:cell division site; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0032174; C:cellular bud neck septin collar; IDA:SGD.
DR GO; GO:0032177; C:cellular bud neck split septin rings; IDA:SGD.
DR GO; GO:0005621; C:cellular bud scar; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0007120; P:axial cellular bud site selection; IMP:SGD.
DR GO; GO:0045184; P:establishment of protein localization; IMP:SGD.
DR GO; GO:0140014; P:mitotic nuclear division; IPI:SGD.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..407
FT /note="Protein NIS1"
FT /id="PRO_0000203447"
FT REGION 41..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 391..398
FT /note="SUMO-binding"
FT COMPBIAS 277..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 407 AA; 45908 MW; 925C7B6063BCE4F1 CRC64;
METYETSIGT QSYPPTLFPP PLGTGGFTTS GYIHALVDST SNSNSNSNTN SNTNSNTNSN
SDTKIPIVQI SDDSHITHDS FKPYMEYHDA SHLRNRNISK ADQVESTEVM EQFTQWSNYK
MRSRSPTINA KPIRHTSQRR TDFTSKNELS KFSKNHNFIF HKGFLKRQHS IRREDRQAKV
RSRFRSKKEL TSVLNYIELE QMDIANVLAS QPVNLHAIRN LTSRDPAVTP IPFLRSQMYA
TSSRPPYLRN RSISRKLPKS QPGSLPTTMP ATATKTIKQN STTPTTRSVY NKNVGRSNTS
PSVLYHPKRR GKLNTKSHAR KEQLLLELWR EYLMLVITQR TQLRLTLLCS PGSASNESSV
CSSNASDLDM SLLSTPSSLF QMAGETKSNP IIIPDSQDDS ILSSDPF
